Structural highlights
Function
A0A2V3F1A3_PSEAI RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.[HAMAP-Rule:MF_00436]
Publication Abstract from PubMed
The widely occurring bacterial RNA chaperone Hfq is a key factor in the post-transcriptional control of hundreds of genes in Pseudomonas aeruginosa. How this broadly acting protein can contribute to the regulatory requirements of many different genes remains puzzling. Here, we describe cryo-EM structures of higher order assemblies formed by Hfq and its partner protein Crc on control regions of different P. aeruginosa target mRNAs. Our results show that these assemblies have mRNA-specific quaternary architectures resulting from the combination of multivalent protein-protein interfaces and recognition of patterns in the RNA sequence. The structural polymorphism of these ribonucleoprotein assemblies enables selective translational repression of many different target mRNAs. This system elucidates how highly complex regulatory pathways can evolve with a minimal economy of proteinogenic components in combination with RNA sequence and fold.
Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.,Dendooven T, Sonnleitner E, Blasi U, Luisi BF EMBO J. 2022 Dec 12:e111129. doi: 10.15252/embj.2022111129. PMID:36504222[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dendooven T, Sonnleitner E, Blasi U, Luisi BF. Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding. EMBO J. 2022 Dec 12:e111129. doi: 10.15252/embj.2022111129. PMID:36504222 doi:http://dx.doi.org/10.15252/embj.2022111129
